ID E0NEA9_PEDAC Unreviewed; 836 AA.
AC E0NEA9;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=ATP-dependent RecD-like DNA helicase {ECO:0000256|HAMAP-Rule:MF_01488};
DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_01488};
GN Name=recD {ECO:0000313|EMBL:EFL96568.1};
GN Synonyms=recD2 {ECO:0000256|HAMAP-Rule:MF_01488};
GN ORFNames=HMPREF0623_0619 {ECO:0000313|EMBL:EFL96568.1};
OS Pediococcus acidilactici DSM 20284.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus; Pediococcus acidilactici group.
OX NCBI_TaxID=862514 {ECO:0000313|EMBL:EFL96568.1, ECO:0000313|Proteomes:UP000004470};
RN [1] {ECO:0000313|EMBL:EFL96568.1, ECO:0000313|Proteomes:UP000004470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20284 {ECO:0000313|EMBL:EFL96568.1,
RC ECO:0000313|Proteomes:UP000004470};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-dependent ATPase and ATP-dependent 5'-3' DNA helicase.
CC Has no activity on blunt DNA or DNA with 3'-overhangs, requires at
CC least 10 bases of 5'-ssDNA for helicase activity. {ECO:0000256|HAMAP-
CC Rule:MF_01488}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01488};
CC -!- SIMILARITY: Belongs to the RecD family. RecD-like subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01488}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFL96568.1}.
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DR EMBL; AEEG01000002; EFL96568.1; -; Genomic_DNA.
DR RefSeq; WP_004165978.1; NZ_GL397067.1.
DR AlphaFoldDB; E0NEA9; -.
DR eggNOG; COG0507; Bacteria.
DR HOGENOM; CLU_007524_0_1_9; -.
DR Proteomes; UP000004470; Unassembled WGS sequence.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd17933; DEXSc_RecD-like; 1.
DR CDD; cd18809; SF1_C_RecD; 1.
DR Gene3D; 1.10.10.2220; -; 1.
DR Gene3D; 2.30.30.940; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_01488; RecD_like; 1.
DR InterPro; IPR006345; DNA_helicase_RecD-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029493; RecD-like_HHH.
DR InterPro; IPR041451; RecD-like_SH13.
DR InterPro; IPR027785; UvrD-like_helicase_C.
DR NCBIfam; TIGR01448; recD_rel; 1.
DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR PANTHER; PTHR43788:SF6; RECBCD ENZYME SUBUNIT RECD; 1.
DR Pfam; PF13604; AAA_30; 1.
DR Pfam; PF14490; HHH_4; 1.
DR Pfam; PF18335; SH3_13; 1.
DR Pfam; PF13538; UvrD_C_2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01488}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_01488};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_01488, ECO:0000313|EMBL:EFL96568.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488, ECO:0000313|EMBL:EFL96568.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}; Reference proteome {ECO:0000313|Proteomes:UP000004470}.
FT DOMAIN 171..261
FT /note="RecD helicase-like helix-hairpin-helix"
FT /evidence="ECO:0000259|Pfam:PF14490"
FT DOMAIN 597..667
FT /note="RecD-like DNA helicase SH3"
FT /evidence="ECO:0000259|Pfam:PF18335"
FT DOMAIN 684..731
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13538"
FT REGION 764..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 374..378
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 836 AA; 92223 MW; AA5119B9CC72515E CRC64;
MAFEKLNLFG DEGSAAPPKK ATSMNKMVEL TGTVNAVFFE SPTSLFKVVL IDVVDQDFDW
KEPQIVVTGN MAEVQEGAKY QFKGKLVEHP KYGTQIQLSQ ASRLGPDTKE GLVEYFAGSQ
FKGIGKKTAE KIVKQLGMDA IDVIKDNAQV LRDIGLSSAQ ADVIETVLAE SNGMEKILIK
LADLGISGKT ADNVIAKYRE DTLKIIEENP YQLANDIENI GFKRVDAIGQ QLNFPVDFPG
RLQSGILATI QEWCNSTGDT YMVAEIMLQR AQQLLGNEIN AEKIAEQVLE LGKQGRVVGE
NGQIYLKWLY QAEEAIGYQL QHLLKNPPKV NEKAVDRAIK RAEEHLALEY DETQNNAIRM
ALSHGITIIT GGPGTGKTTI VKGLINSFAE LHDLDLDPNA NPDQDYPIQL AAPTGRAAKR
LSEVTGVPAK TIHRLLGLNG NDDLHDEQIQ ELRGELLVVD EMSMVDTGLF NTLISAINAE
MQVVLVGDKD QLPSVGPGQV FSDLIRSQKI PTISLTKIYR QEQDSSIIQM AHSIQNGEMP
DDFTQNRPDK SFIKTSAYQV ADAIDQIAER AVARGLSKND LQVLAPMYRG AAGIDEINRH
LQRVLNPPQT DHPKYLEANH QQFRIGDKVL QLVNAPENNI FNGDIGEITG IVTEKAGKGH
AQLIVDYDGN EVTYGKNDLN QLTLAYCVSI HKSQGSEFPV VILPMVRQYY RMLQRNLLYT
GLTRASDSII LLGEVEAYQR AVQNESANRQ TGLVKRLNPE IAITEKPIAE KSEPKTTSEK
SEAGEPQRKS ILTKPEVTET FATSGDEPTL LTKQLVETGK IDPMIGMDGV TPRDFL
//
